This laboratory has studied the amino acid sequence of several species of luteinizing hormone (ovine, bovine, porcine, human). We are now turning our attention to the sequence of the carbohydrate moieties on these preparations. A statistical approach based on specificity of glycosidases (several are required) and sequence of release of sugars from the non-reducing end(s) is being employed. This method is advantageous in that small quantities of glycopeptide are required. Eventually chemical procedures will also be used to resolve points of ambiguity. Other studies concern the placement of the disulfide bonds in ovine luteinizing hormone. The mechanism of action of luteinizing hormone is being studied with respect to the interaction of the hormone with the receptor site and the activation of adenyl cyclase.